Evidence map›Paper›PMID 23386612›Full record

ArticleThe Journal of biological chemistry2013

Secreted trypanosome cyclophilin inactivates lytic insect defense peptides and induces parasite calcineurin activation and infectivity.

Manjusha M Kulkarni, Anna Karafova, Wojciech Kamysz, Sergio Schenkman, Roger Pelle, Bradford S McGwire

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Pathogens (Basel, Switzerland) · 2025
    Review
  5. Article
  6. Insights into Peptidyl-ProlylPathogens (Basel, Switzerland) · 2024
    Review
  7. Interaction ofMicroorganisms · 2024
    Review
  8. International journal of molecular sciences · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Parasitology · 2021
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Microbial cyclophilins: specialized functions in virulence and beyond.World journal of microbiology & biotechnology · 2017
    Review
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 5 institutions in 4 countries.

Manjusha M KulkarniCenter for Microbial Interface Biology, The Ohio State University Medical Center, Columbus, Ohio 43210.
Anna KarafovaFaculty of Pharmacy, Medical University of Gdansk, 80-120 Gdansk, Poland.
Wojciech KamyszFaculty of Pharmacy, Medical University of Gdansk, 80-120 Gdansk, Poland.
Sergio SchenkmanDepartamento de Microbiologia, Imunologia e Parasitologia-Universidade Federal de Sao Paulo, 04023-062 SP, Brazil.
Roger PelleInternational Livestock Research Institute, Nairobi 00100, Kenya.
Bradford S McGwireCenter for Microbial Interface Biology, The Ohio State University Medical Center, Columbus, Ohio 43210; Division of Infectious Diseases, The Ohio State University Medical Center, Columbus, Ohio 43210. Electronic address: brad.mcgwire@osumc.edu.
Gdańsk Medical University · PLInterface (United States) · USInternational Livestock Research Institute · KEThe Ohio State University · USUniversidade Federal de São Paulo · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanisms by which Trypanosoma cruzi survives antimicrobial peptides and differentiates during its transit through the gastrointestinal tract of the reduviid vector are unknown. We show that cyclophilin, a peptidyl-prolyl isomerase secreted from T. cruzi epimastigotes, binds to and neutralizes the reduviid antimicrobial peptide trialysin promoting parasite survival. This is dependent on a singular proline residue in trialysin and is inhibited by the cyclophilin inhibitor cyclosporine A. In addition, cyclophilin-trialysin complexes enhance the production of ATP and reductase responses of parasites, which are inhibited by both calcineurin-specific inhibitors cyclosporine A and FK506. Calcineurin phosphatase activity of cyclophilin-trialysin-treated parasites was higher than in controls and was inhibited by preincubation by either inhibitor. Parasites exposed to cyclophilin-trialysin have enhanced binding and invasion of host cells leading to higher infectivity. Leishmanial cyclophilin also mediates trialysin protection and metabolic stimulation by T. cruzi, indicating that extracellular cyclophilin may be critical to adaptation in other insect-borne protozoa. This work demonstrates that cyclophilin serves as molecular sensor leading to the evasion and adaptive metabolic response to insect defense peptides.

Indexed as

Adaptation, BiologicalAdenosine TriphosphateAmino Acid SequenceAnimalsCalcineurinCell LineCyclophilinsEnergy MetabolismEnzyme ActivationHost-Parasite InteractionsImmune EvasionLeishmaniaMitochondriaMolecular Sequence DataOxidoreductasesProlineAdenosine TriphosphateCalcineurincyclophilin 19CyclophilinsOxidoreductasesprolinalProlineProtozoan ProteinsSalivary Proteins and Peptidestrialysin protein, Triatoma infestans

Identifiers

PMID23386612
PMCPMC3605694
OpenAlexW2060926320

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.